A0A832S687 · A0A832S687_9EURY

  • Protein
    CTP synthase
  • Gene
    pyrG
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.

Miscellaneous

CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Activity regulation

Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site12CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site12UTP (UniProtKB | ChEBI)
Binding site13-18ATP (UniProtKB | ChEBI)
Binding site53L-glutamine (UniProtKB | ChEBI)
Binding site70ATP (UniProtKB | ChEBI)
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site140Mg2+ (UniProtKB | ChEBI)
Binding site147-149CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site186-191UTP (UniProtKB | ChEBI)
Binding site222CTP (UniProtKB | ChEBI); allosteric inhibitor
Binding site222UTP (UniProtKB | ChEBI)
Binding site240ATP (UniProtKB | ChEBI)
Binding site352L-glutamine (UniProtKB | ChEBI)
Active site379Nucleophile
Active site379Nucleophile; for glutamine hydrolysis
Binding site380-383L-glutamine (UniProtKB | ChEBI)
Binding site403L-glutamine (UniProtKB | ChEBI)
Binding site460L-glutamine (UniProtKB | ChEBI)
Active site503
Active site505

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCTP synthase activity
Molecular Functionmetal ion binding
Biological Process'de novo' CTP biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CTP synthase
  • EC number
  • Alternative names
    • Cytidine 5'-triphosphate synthase
    • Cytidine triphosphate synthetase
      (CTP synthetase
      ; CTPS
      )
    • UTP--ammonia ligase

Gene names

    • Name
      pyrG
    • ORF names
      HA306_02525

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • UBA8098
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina

Accessions

  • Primary accession
    A0A832S687

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-265Amidoligase domain
Domain2-265CTP synthase N-terminal
Domain300-522Glutamine amidotransferase

Sequence similarities

Belongs to the CTP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    534
  • Mass (Da)
    59,775
  • Last updated
    2021-09-29 v1
  • Checksum
    F488F21D4B951967
MKYIVVTGGVMSGLGKGITIASIGRNLKNKGYKVTAIKIDPYINIDAGTMSPYQHGEVFVLRDGGEVDLDLGNYERFLDTELTRDHNLTTGKVYQEVIAKERRGDYLGKTVQIIPHITNEIKNKIRKVAARSGADICLVEIGGTVGDIESMPFLEAVRQMHREEPSENIVFIHVTLVMEDLQGEQKTKPSQHSVKELRALGLSPEVIVARSKTPLQDSAKEKIALFCDVPQELVISAYDADDIYDVPLSIEEQGLTSRLMKHLRLDSCVEDNGWREMVARMKSTTDEVKLAIVGKYTNLEDSYLSILEAVKHGGIDNVCKVEVNMVEAETLEEDPAEVEKLKKYDGILIPGGFGGRGTEGKMLAIKFARENDIPFLGICLGMQLAVIEFARNVANLENANSTEFDEDTPYPVIDILPEQTGVADMGGTMRLGDYDAILKESSIATRLYGTNYIVERHRHRYEVNPEFVDRLESFGIVFSGKNKNRMEIAEIPDKRFFFASQFHPEFKSRPGRPSPPFKGLVQAMCKYRKEKESQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DUIO01000074
EMBL· GenBank· DDBJ
HIH74169.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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